Recognizing and remodeling the nucleosome

被引：22

作者：

Glatt, Sebastian ^{[1
]}

Alfieri, Claudio ^{[1
]}

Mueller, Christoph W. ^{[1
]}

机构：

[1] European Mol Biol Lab, Struct & Computat Biol Unit, D-69117 Heidelberg, Germany

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2011年 / 21卷 / 03期

关键词：

HISTONE H3 TAIL; CORE PARTICLE; CHROMATIN MODIFICATIONS; ANGSTROM RESOLUTION; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; PHD FINGER; RECOGNITION; COMPLEX; BROMODOMAIN;

D O I：

10.1016/j.sbi.2011.02.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The X-ray structure of the nucleosome core particle (NCP) has been a major milestone in the structural biology of chromatin. Since, our understanding how NCPs interact with multiple partners has been extending from single chromatin-binding domains recognizing post-translational modifications (PTMs) in histone tails towards the recognition of higher-order chromatin structure by multi-subunit chromatin remodeling complexes. The current review summarizes recent progress in the structural biology of nucleosome-recognition from chromatin-binding domains to multi-protein remodeling complexes.

引用

页码：335 / 341

页数：7

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